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MAbs 8H2, 6F12 and 7C7 were tested against different preparations of other fungal antigens and reacted distinctly, suggesting binding to unique epitopes.
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However, most antibodies do not bind to unique epitopes and so they will cross-react.
The distinction of ofatumumab with regard to CDC induction was found to be linked to binding to a unique epitope on CD20 [ 35].
The layer formation seems to hinder aPL binding to β2GPI epitopes close to D5 [16].
Both the mouse 13H11 MAb and the three prototypic cluster II human MAbs (98-6, 126-6, and 167-D) blocked 2F5 binding to gp41 epitopes to variable degrees; the combination of 98-6 and 13H11 completely blocked 2F5 binding.
Epitope mapping was performed with all antibodies to verify binding to linear epitopes.
ICR65, however, cross-reacted with mAbs binding to both epitopes.
Ligands binding to distinct epitopes on the same target molecule may influence each other, for example, inhibiting binding to adjacent epitopes.
The competitive inhibition of binding to overlapping epitopes has been described for antibodies to ACE.
Ligands binding to distinct epitopes of anchoring molecules may enter cells differently.
The inhibition is mediated via antibody binding to epitopes outside of the CD81 binding site in E2, possibly by preventing conformational changes in E2 that are required for CD81 binding.
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